P24664 (TRYP_SACER) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Trypsin EC=3.4.21.4 Alternative name(s): SET
Organism	Saccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifier	1836 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Miscellaneous	Hardly autolyzes itself at all at its active pH range.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 227	227	Trypsin		PRO_0000088718
Regions
	Domain	1 – 223	223	Peptidase S1
Sites
	Active site	42	1	Charge relay system
	Active site	88	1	Charge relay system
	Active site	179	1	Charge relay system
	Site	173	1	Required for specificity By similarity
Amino acid modifications
	Disulfide bond	27 ↔ 43
	Disulfide bond	150 ↔ 164
	Disulfide bond	175 ↔ 199

Sequences

	Sequence		Length	Mass (Da)
	P24664 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: D5AC5E47B227B418	FASTA	227	23,308
	10 20 30 40 50 60 IVGGEDANVQ DHPFTVALVT PDGQQFCGGT LAAPNKVVTA AHCTVGSQPA DINVVSGRTV 70 80 90 100 110 120 MSSNIGTVSK VTNVWVHPEY QDAAKGFDVS VLTLEAPVKE APIELAKADD AGYAPDTAAT 130 140 150 160 170 180 ILGWGNTSEG GQQADHLQKA TVPVNSDDTC KQAYGEYTPN AMVCAGVPEG GVDTCQGDSG 190 200 210 220 GPMVVNNKLI GVTSWGEGCA RPGKPGVYAR VGAYYDVLME QINAGAV

References

[1]	Miyamoto K., Matsuo H., Narita K. (In) Proceedings of Dai 30 kai tanpakushitsu kouzou touronkai kouen youshishuu, pp.77-80, Tokyo (1979) Cited for: PROTEIN SEQUENCE.
[2]	"Crystal structure of Streptomyces erythraeus trypsin at 2.7-A resolution." Yamane T., Kobuke M., Tsutsui H., Toida T., Suzuki A., Ashida T., Kawata Y., Sakiyama F. J. Biochem. 110:945-950(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SEQUENCE REVISION.

Cross-references

3D structure databases
ProteinModelPortal	P24664.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-8289191.
Protein family/group databases
MEROPS	S01.102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRYP_SACER

Accession

Primary (citable) accession number: P24664

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	May 29, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program